Research workbench
Crystal structure of chaetomium thermophilum GLE1 ctd-NUP42 gbm complex
Analyse Crystal structure of chaetomium thermophilum GLE1 ctd-NUP42 gbm complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B4G
- Type
- protein
- Length
- 1,439 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoporin GLE1; Nucleoporin AMO1
- UniProt
- G0S7F3, G0S381
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 7 distinct chains · 64% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoporin GLE1 | protein | 315 | 65% helix, 3% strand | G0S7F3 |
| B | Nucleoporin AMO1 | protein | 47 | 47% helix, 0% strand | G0S381 |
| D, F | Nucleoporin AMO1 | protein | 50 | 42% helix, 0% strand | G0S381 |
| H | Nucleoporin AMO1 | protein | 45 | 47% helix, 0% strand | G0S381 |
| C | Nucleoporin GLE1 | protein | 310 | 67% helix, 3% strand | G0S7F3 |
| E | Nucleoporin GLE1 | protein | 314 | 64% helix, 3% strand | G0S7F3 |
| G | Nucleoporin GLE1 | protein | 308 | 67% helix, 3% strand | G0S7F3 |
Ligands and binding sites
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 5 copies · chains A, C, E, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 968 | 0.79 | 0.81 | 89 | empty |
| 2 | 958 | 0.70 | 0.75 | 69 | empty |
| 3 | 646 | 0.65 | 0.75 | 69 | MES |
| 4 | 337 | 0.59 | 0.77 | 37 | empty |
| 5 | 284 | 0.56 | 0.76 | 40 | empty |
Interfaces
10 interfaces between chains.
- D–C · 1003 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 995 Ų buried · 12 hydrogen bonds · protein-protein
- F–E · 948 Ų buried · 12 hydrogen bonds · protein-protein
- H–G · 874 Ų buried · 9 hydrogen bonds · protein-protein
- A–E · 441 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt G0S7F3
- Every structure of UniProt G0S381
- Elsewhere: RCSB PDB 6B4G · PDBe 6B4G · UniProt G0S7F3 · UniProt G0S381
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